Comamonas (previously Pseudomonas) sp. NCIMB 9872 was one of the few microorganisms that have been characterized to produce a Baeyer-Villiger monooxygenase (BVMO; Griffin, M., et al., Biochem. J. 129:595–603, 1972; Griffin, M., et al., Eur. J. Biochem. 63:199–209, 1976; and Willetts, A., Trends in Biotech. 15:55–62, 1997; for a recent review). BVMOs are flavoproteins that mimic the classical Baeyer-Villiger organic chemical reaction which is a peracid-catalyzed oxidation of a ketone to an ester or lactone. The use of enzyme substitutes for the production of lactones in high yield and optical purity is an attractive feature in current trends of research and development toward replacing chemical methods with biological alternatives (Stinson, S. C., Chem. Eng. News, 83–104, 1998). To date, the best characterized BVMO enzyme is that of cyclohexanone monooxygenase (CHMO) produced by Acinetobacter sp. NCIMB 9871 (Stewart, J. D., Curr. Org. Chem. 2:195–216, 1998; Willetts, A., Trends in Biotech. 15:55–62, 1997). This is also the only BVMO whose gene has been cloned and sequenced (Chen, et al., J. Bacteriol. 170:781–789, 1988). Recently, this valuable resource was used to engineer a “designer yeast” in a whole-cell approach to effect a variety of asymmetric Baeyer-Villiger oxidations (Stewart, J. D., et al., J. Am. Chem. Soc. 120:3541–3548, 1998).
It would be highly desirable to be provided with a new CPMO having an increased enzymatic activity for growing cells in a medium containing cyclopentanol or cyclopentanone as sole carbon source.